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Protein

Paxillin

Gene

Pxn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).By similarity

GO - Molecular functioni

  • beta-catenin binding Source: MGI
  • BH4 domain binding Source: MGI
  • receptor signaling complex scaffold activity Source: MGI
  • vinculin binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • branching morphogenesis of an epithelial tube Source: MGI
  • cytoskeleton organization Source: MGI
  • focal adhesion assembly Source: MGI
  • growth hormone receptor signaling pathway Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • lamellipodium assembly Source: MGI
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of protein kinase activity Source: MGI
  • regulation of cell shape Source: MGI
  • substrate adhesion-dependent cell spreading Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-180292. GAB1 signalosome.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445355. Smooth Muscle Contraction.
R-MMU-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Names & Taxonomyi

Protein namesi
Recommended name:
Paxillin
Gene namesi
Name:Pxn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:108295. Pxn.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cell junctionfocal adhesion By similarity
  • Cytoplasmcell cortex 1 Publication

  • Note: Colocalizes with integrins at the cell periphery. Colocalizes with PXN to membrane ruffles and the leading edge of migrating cells (By similarity).By similarity

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cell leading edge Source: MGI
  • cytoplasm Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: MGI
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
  • stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000758541 – 591PaxillinAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei31Phosphotyrosine; by PTK6By similarity1
Modified residuei83PhosphoserineCombined sources1
Modified residuei88PhosphotyrosineCombined sources1
Modified residuei106PhosphoserineBy similarity1
Modified residuei118Phosphotyrosine; by PTK6Combined sources1 Publication1
Modified residuei119PhosphoserineBy similarity1
Modified residuei126PhosphoserineCombined sources1
Modified residuei130PhosphoserineCombined sources1
Modified residuei132PhosphothreonineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Modified residuei140PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei181PhosphotyrosineBy similarity1
Modified residuei230PhosphoserineBy similarity1
Modified residuei244Phosphoserine; by CDK5By similarity1
Modified residuei250PhosphoserineBy similarity1
Modified residuei258PhosphoserineBy similarity1
Modified residuei261PhosphoserineBy similarity1
Modified residuei272PhosphoserineCombined sources1
Modified residuei303PhosphoserineBy similarity1
Modified residuei322PhosphoserineCombined sources1
Modified residuei332PhosphoserineBy similarity1
Modified residuei340PhosphoserineCombined sources1
Modified residuei533PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by MAPK1/ERK2. Phosphorylated on tyrosine residues during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens. Phosphorylation at Ser-244 by CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation (By similarity). Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion (By similarity). Phosphorylation at Ser-250 by SLK is required for PXN redistribution and cell motility (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8VI36.
PeptideAtlasiQ8VI36.
PRIDEiQ8VI36.

PTM databases

iPTMnetiQ8VI36.
PhosphoSitePlusiQ8VI36.

Miscellaneous databases

PMAP-CutDBQ8VI36.

Expressioni

Gene expression databases

BgeeiENSMUSG00000029528.
CleanExiMM_PXN.
ExpressionAtlasiQ8VI36. baseline and differential.
GenevisibleiQ8VI36. MM.

Interactioni

Subunit structurei

Interacts with VCL and SRC (via SH3 domain). Interacts with GIT1, NUDT16L1/SDOS and TGFB1I1. Component of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and PAK1. Binds ASAP2. Interacts with RNF5 and PDCD10 (By similarity). Interacts with SORBS1, PARVA and PARVB. Interacts with NEK3 and this interaction is prolactin-dependent (By similarity). Interacts with PTK2/FAK1. Interacts with PTK6 (By similarity). Interacts with PTK2B/PYK2. Interacts with CD36. Interacts (via cytoplasmic domain) with CEACAM1; the interaction is phosphotyrosyl-dependent (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
L1camP116272EBI-983394,EBI-397964
Ptk2P341523EBI-983394,EBI-77070
PTPN1P180312EBI-983394,EBI-968788From a different organism.
VclQ647273EBI-983394,EBI-432047

GO - Molecular functioni

  • beta-catenin binding Source: MGI
  • BH4 domain binding Source: MGI
  • receptor signaling complex scaffold activity Source: MGI
  • vinculin binding Source: MGI

Protein-protein interaction databases

BioGridi202525. 17 interactors.
IntActiQ8VI36. 20 interactors.
MINTiMINT-141924.
STRINGi10090.ENSMUSP00000083709.

Structurei

3D structure databases

ProteinModelPortaliQ8VI36.
SMRiQ8VI36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini356 – 415LIM zinc-binding 1PROSITE-ProRule annotationAdd BLAST60
Domaini416 – 473LIM zinc-binding 2PROSITE-ProRule annotationAdd BLAST58
Domaini474 – 533LIM zinc-binding 3PROSITE-ProRule annotationAdd BLAST60
Domaini534 – 591LIM zinc-binding 4PROSITE-ProRule annotationAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 15LD motif 1Add BLAST13
Motifi144 – 156LD motif 2Add BLAST13
Motifi216 – 228LD motif 3Add BLAST13
Motifi265 – 276LD motif 4Add BLAST12
Motifi333 – 345LD motif 5Add BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi46 – 53Pro-rich8

Sequence similaritiesi

Belongs to the paxillin family.Curated
Contains 4 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ8VI36.
KOiK05760.
PhylomeDBiQ8VI36.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24216:SF11. PTHR24216:SF11. 1 hit.
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta (identifier: Q8VI36-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDLDALLAD LESTTSHISK RPVFLSEEPP YSYPTGNHTY QEIAVPPPVP
60 70 80 90 100
PPPSSEALNG TVLDPLDQWQ PSGSRYAHQQ PPSPLPVYSS SAKNSSASNT
110 120 130 140 150
QDGVGSLCSR AGEEEHVYSF PNKQKSAEPS PTVMSSSLGS NLSELDRLLL
160 170 180 190 200
ELNAVQHSPP GFPADEAESS PPLPGALSPL YGIPENNTPL GGKAGPLVKE
210 220 230 240 250
KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS
260 270 280 290 300
SQQQTRISAS SATRELDELM ASLSDFKMQG LEQRVDGERP WAAGWPPSSR
310 320 330 340 350
QSSPEGQDEG GFMAQGKTGS SSPPGGLSKP GSQLDSMLGS LQSDLNKLGV
360 370 380 390 400
ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD
410 420 430 440 450
GQPYCEKDYH SLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF
460 470 480 490 500
GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF
510 520 530 540 550
VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM
560 570 580 590
AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQSCFVKLF C
Length:591
Mass (Da):64,476
Last modified:March 1, 2002 - v1
Checksum:iB41A1892E6F60544
GO
Isoform Alpha (identifier: Q8VI36-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     278-311: Missing.

Show »
Length:557
Mass (Da):60,811
Checksum:i483D880CF16289B5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71P → R in BAE42452 (PubMed:16141072).Curated1
Sequence conflicti212D → N in BAE34151 (PubMed:16141072).Curated1
Sequence conflicti294G → S in BAE34151 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_016357278 – 311Missing in isoform Alpha. 2 PublicationsAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293883 mRNA. Translation: AAL71910.1.
AF293882 mRNA. Translation: AAL71909.1.
AK149933 mRNA. Translation: BAE29176.1.
AK157688 mRNA. Translation: BAE34151.1.
AK167299 mRNA. Translation: BAE39404.1.
AK171436 mRNA. Translation: BAE42452.1.
CCDSiCCDS19593.1. [Q8VI36-2]
CCDS39229.1. [Q8VI36-1]
RefSeqiNP_035353.1. NM_011223.3. [Q8VI36-2]
NP_598676.2. NM_133915.3.
UniGeneiMm.18714.

Genome annotation databases

EnsembliENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528. [Q8VI36-2]
GeneIDi19303.
KEGGimmu:19303.
UCSCiuc008zeb.2. mouse. [Q8VI36-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293883 mRNA. Translation: AAL71910.1.
AF293882 mRNA. Translation: AAL71909.1.
AK149933 mRNA. Translation: BAE29176.1.
AK157688 mRNA. Translation: BAE34151.1.
AK167299 mRNA. Translation: BAE39404.1.
AK171436 mRNA. Translation: BAE42452.1.
CCDSiCCDS19593.1. [Q8VI36-2]
CCDS39229.1. [Q8VI36-1]
RefSeqiNP_035353.1. NM_011223.3. [Q8VI36-2]
NP_598676.2. NM_133915.3.
UniGeneiMm.18714.

3D structure databases

ProteinModelPortaliQ8VI36.
SMRiQ8VI36.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202525. 17 interactors.
IntActiQ8VI36. 20 interactors.
MINTiMINT-141924.
STRINGi10090.ENSMUSP00000083709.

PTM databases

iPTMnetiQ8VI36.
PhosphoSitePlusiQ8VI36.

Proteomic databases

PaxDbiQ8VI36.
PeptideAtlasiQ8VI36.
PRIDEiQ8VI36.

Protocols and materials databases

DNASUi19303.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067268; ENSMUSP00000069624; ENSMUSG00000029528. [Q8VI36-2]
GeneIDi19303.
KEGGimmu:19303.
UCSCiuc008zeb.2. mouse. [Q8VI36-2]

Organism-specific databases

CTDi5829.
MGIiMGI:108295. Pxn.

Phylogenomic databases

eggNOGiKOG1703. Eukaryota.
ENOG410XRD4. LUCA.
GeneTreeiENSGT00760000118910.
HOGENOMiHOG000018764.
HOVERGENiHBG001512.
InParanoidiQ8VI36.
KOiK05760.
PhylomeDBiQ8VI36.

Enzyme and pathway databases

ReactomeiR-MMU-180292. GAB1 signalosome.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445355. Smooth Muscle Contraction.
R-MMU-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Miscellaneous databases

ChiTaRSiPxn. mouse.
PMAP-CutDBQ8VI36.
PROiQ8VI36.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029528.
CleanExiMM_PXN.
ExpressionAtlasiQ8VI36. baseline and differential.
GenevisibleiQ8VI36. MM.

Family and domain databases

Gene3Di2.10.110.10. 4 hits.
InterProiIPR001904. Paxillin.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR24216:SF11. PTHR24216:SF11. 1 hit.
PfamiPF00412. LIM. 4 hits.
[Graphical view]
SMARTiSM00132. LIM. 4 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 4 hits.
PS50023. LIM_DOMAIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAXI_MOUSE
AccessioniPrimary (citable) accession number: Q8VI36
Secondary accession number(s): Q3TB62, Q3TZQ6, Q8VI37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.